Investigation of the Effects of 1,2,4-Triazole and Thiazole Ring-Containing Hybrid Molecules on Carbonic Anhydrase I and II

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dc.contributor.authorCamadan, Yasemin
dc.contributor.authorAkkemik, Ebru
dc.contributor.authorGuller, Pinar
dc.contributor.authorCeylan, Sule
dc.contributor.authorOzdemir, Hasan
dc.date.accessioned2024-12-24T19:24:21Z
dc.date.available2024-12-24T19:24:21Z
dc.date.issued2024
dc.departmentSiirt Üniversitesi
dc.description.abstractCarbonic anhydrase (CA, EC 4.2.1.1) is an enzyme that catalyzes the reversible reaction of carbon dioxide to bicarbonate and a proton under physiological conditions. Pharmaceutical research has gained importance since the design of novel compounds that inhibit CA I-II isoenzymes has a promising approach for pharmacological intervention in many diseases. Triazole derivatives have attracted attention due to their chemotherapeutic, antifungal, antiviral, antibiotic, analgesic, and antifungal activities. Therefore, in this study, the effect of 1,2,4-triazole and thiazole ring-containing compounds on human carbonic anhydrase I (hCA I) and II (hCA II) isoenzymes were investigated in vitro. For this purpose, hCA I and hCA II isoenzymes were purified by Sepharose-4B affinity column chromatography. Estimation of inhibition mechanism and drug-likeness characteristics of compounds were also determined using molecular docking simulation. The inhibitory effects of ten compounds were investigated. Activity vs. concentration graphs were prepared for each compound and IC50 values or AC50 were calculated from these graphs. It was revealed that some of the compounds exhibited selective inhibition on carbonic anhydrase isoenzymes. The studied compounds are considered to be drug candidates. 1,2,4-triazole and thiazole ring-containing hybrid molecules inhibited hCA-I isoenzyme with IC50 values between 0.135 and 0.523 mM and hCA II with IC50 values between 0.108 and 0.523 mM. Molecule 8 showed the highest inhibition potency against hCA-I while molecule 3 showed the highest inhibitory effect against hCA-II. Estimated binding energies for molecule 10 into hCA I is -9.31 kcal/mol and for molecule 2 on hCA II is -8.21 kcal/mol. image
dc.description.sponsorshipArtvin Coruh University Scientific Research Projects Coordination Office (ACUBAP); [2015.m80.02.01]
dc.description.sponsorshipA part of this study was supported by Artvin Coruh University Scientific Research Projects Coordination Office (ACUBAP) with project No: 2015.m80.02.01.
dc.identifier.doi10.1002/slct.202303236
dc.identifier.issn2365-6549
dc.identifier.issue6
dc.identifier.scopus2-s2.0-85185111712
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1002/slct.202303236
dc.identifier.urihttps://hdl.handle.net/20.500.12604/5937
dc.identifier.volume9
dc.identifier.wosWOS:001159758000001
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherWiley-V C H Verlag Gmbh
dc.relation.ispartofChemistryselect
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_20241222
dc.subjectcarbonic anhydrase
dc.subjectenzyme inhibition
dc.subjectmolecular docking
dc.subjectADMET
dc.titleInvestigation of the Effects of 1,2,4-Triazole and Thiazole Ring-Containing Hybrid Molecules on Carbonic Anhydrase I and II
dc.typeArticle

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